RING1

From Wikipedia, the free encyclopedia

Ring finger protein 1

PDB rendering based on 2h0d.

Available structures: 2h0d

Identifiers

Symbol(s)

RING1; RNF1

External IDs

OMIM: 602045 MGI: 1101770 HomoloGene: 68283

Gene ontology
Molecular Function:	• chromatin binding • ubiquitin-protein ligase activity • protein binding • zinc ion binding • transcription repressor activity • ligase activity • metal ion binding
Cellular Component:	• ubiquitin ligase complex • sex chromatin • nucleus • nuclear body • PcG protein complex
Biological Process:	• transcription • regulation of transcription, DNA-dependent • ubiquitin cycle • anterior/posterior pattern formation • chromatin modification • histone ubiquitination

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002931 (mRNA)
NP_002922 (protein)

NM_009066 (mRNA)
NP_033092 (protein)

Location

Chr 6: 33.28 - 33.29 Mb

Chr 17: 33.63 - 33.64 Mb

Pubmed search

[1]

[2]

Ring finger protein 1, also known as RING1, is a human gene.^[1]

This gene belongs to the RING finger family, members of which encode proteins characterized by a RING domain, a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is associated with the multimeric polycomb group protein complex. The gene product interacts with the polycomb group proteins BMI1, EDR1, and CBX4, and colocalizes with these proteins in large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is contiguous with the RING finger genes FABGL and HKE4.^[1]

[edit] References

^ ^a ^b Entrez Gene: RING1 ring finger protein 1.

[edit] Further reading

Hanson IM, Poustka A, Trowsdale J (1991). "New genes in the class II region of the human major histocompatibility complex.". Genomics 10 (2): 417-24. PMID 1906426.
Lovering R, Hanson IM, Borden KL, et al. (1993). "Identification and preliminary characterization of a protein motif related to the zinc finger.". Proc. Natl. Acad. Sci. U.S.A. 90 (6): 2112-6. PMID 7681583.
Satijn DP, Gunster MJ, van der Vlag J, et al. (1997). "RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor.". Mol. Cell. Biol. 17 (7): 4105-13. PMID 9199346.
Kikuti YY, Tamiya G, Ando A, et al. (1997). "Physical mapping 220 kb centromeric of the human MHC and DNA sequence analysis of the 43-kb segment including the RING1, HKE6, and HKE4 genes.". Genomics 42 (3): 422-35. doi:10.1006/geno.1997.4745. PMID 9205114.
Satijn DP, Otte AP (1999). "RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity.". Mol. Cell. Biol. 19 (1): 57-68. PMID 9858531.
García E, Marcos-Gutiérrez C, del Mar Lorente M, et al. (1999). "RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1.". EMBO J. 18 (12): 3404-18. doi:10.1093/emboj/18.12.3404. PMID 10369680.
Bárdos JI, Saurin AJ, Tissot C, et al. (2000). "HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties.". J. Biol. Chem. 275 (37): 28785-92. doi:10.1074/jbc.M001835200. PMID 10825164.
Trimarchi JM, Fairchild B, Wen J, Lees JA (2001). "The E2F6 transcription factor is a component of the mammalian Bmi1-containing polycomb complex.". Proc. Natl. Acad. Sci. U.S.A. 98 (4): 1519-24. doi:10.1073/pnas.041597698. PMID 11171983.
Dahiya A, Wong S, Gonzalo S, et al. (2001). "Linking the Rb and polycomb pathways.". Mol. Cell 8 (3): 557-69. PMID 11583618.
Ogawa H, Ishiguro K, Gaubatz S, et al. (2002). "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells.". Science 296 (5570): 1132-6. doi:10.1126/science.1069861. PMID 12004135.
Akasaka T, Takahashi N, Suzuki M, et al. (2003). "MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation.". Genes Cells 7 (8): 835-50. PMID 12167161.
Levine SS, Weiss A, Erdjument-Bromage H, et al. (2002). "The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans.". Mol. Cell. Biol. 22 (17): 6070-8. PMID 12167701.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805-11. doi:10.1038/nature02055. PMID 14574404.
Gil J, Bernard D, Martínez D, Beach D (2004). "Polycomb CBX7 has a unifying role in cellular lifespan.". Nat. Cell Biol. 6 (1): 67-72. doi:10.1038/ncb1077. PMID 14647293.
Obuse C, Yang H, Nozaki N, et al. (2004). "Proteomics analysis of the centromere complex from HeLa interphase cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of the CEN-complex, while BMI-1 is transiently co-localized with the centromeric region in interphase.". Genes Cells 9 (2): 105-20. PMID 15009096.
Wang H, Wang L, Erdjument-Bromage H, et al. (2004). "Role of histone H2A ubiquitination in Polycomb silencing.". Nature 431 (7010): 873-8. doi:10.1038/nature02985. PMID 15386022.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Qin H, Du D, Zhu Y, et al. (2005). "The PcG protein HPC2 inhibits RBP-J-mediated transcription by interacting with LIM protein KyoT2.". FEBS Lett. 579 (5): 1220-6. doi:10.1016/j.febslet.2005.01.022. PMID 15710417.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi:10.1038/nature04209. PMID 16189514.

[edit] External links

MeSH RING1+protein,+human

This article on a gene on chromosome 6 is a stub. You can help Wikipedia by expanding it.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

v • d • e

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1

(1.3) bHLH-ZIP	MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)

(1.6) Basic helix-span-helix (bHSH)	AP-2

(2) Zinc finger
DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)

(2.3) Cys₂His₂	ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2

(3.6) TEA domain	transcriptional enhancer factor 1, 2

(4) β-Scaffold factors with
minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	Rb • RBL1 • RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 • EREBP • B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD

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RING1

From Wikipedia, the free encyclopedia

[edit] References

[edit] Further reading

[edit] External links

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